ID   DHQS_HALMA              Reviewed;         388 AA.
AC   Q5V143;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=3-dehydroquinate synthase {ECO:0000255|HAMAP-Rule:MF_01244};
DE            Short=DHQ synthase {ECO:0000255|HAMAP-Rule:MF_01244};
DE            EC=1.4.1.24 {ECO:0000255|HAMAP-Rule:MF_01244};
DE   AltName: Full=3-dehydroquinate synthase II {ECO:0000255|HAMAP-Rule:MF_01244};
GN   Name=aroB' {ECO:0000255|HAMAP-Rule:MF_01244}; OrderedLocusNames=rrnAC1879;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
CC   -!- FUNCTION: Catalyzes the oxidative deamination and cyclization of 2-
CC       amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3-
CC       dehydroquinate (DHQ), which is fed into the canonical shikimic pathway
CC       of aromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01244}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + H2O + NAD(+)
CC         = 3-dehydroquinate + H(+) + NADH + NH4(+); Xref=Rhea:RHEA:25956,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58859; EC=1.4.1.24; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01244};
CC   -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01244}.
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DR   EMBL; AY596297; AAV46760.1; -; Genomic_DNA.
DR   RefSeq; WP_011223903.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V143; -.
DR   STRING; 272569.rrnAC1879; -.
DR   PRIDE; Q5V143; -.
DR   EnsemblBacteria; AAV46760; AAV46760; rrnAC1879.
DR   GeneID; 40152815; -.
DR   KEGG; hma:rrnAC1879; -.
DR   PATRIC; fig|272569.17.peg.2544; -.
DR   eggNOG; arCOG04353; Archaea.
DR   HOGENOM; CLU_056379_0_0_2; -.
DR   OMA; HFGMAIK; -.
DR   Proteomes; UP000001169; Chromosome I.
DR   GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro.
DR   GO; GO:0102042; F:dehydroquinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01244; Arch_DHQ_synthase; 1.
DR   InterPro; IPR002812; DHQ_synth.
DR   PANTHER; PTHR33563; PTHR33563; 1.
DR   Pfam; PF01959; DHQS; 1.
DR   PIRSF; PIRSF006655; DHQ_synth; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..388
FT                   /note="3-dehydroquinate synthase"
FT                   /id="PRO_1000067063"
SQ   SEQUENCE   388 AA;  42466 MW;  45CA7C7F1BBD6B60 CRC64;
     MTRSVWLKAD SEVGDWETRK RRITAGIEAG VDWVLVDEED VDRVSELGEI NIAAFTNGDV
     HVMEAEAEDS EADATIVGKD GEGDGTVDLP SDFSGSADLS TLRQNGAAPD GGYVRIFDED
     YEAFAEAVAA EADFTIVIGE NWQIIPLENL IARVGEETDL IAGVRTAEDA RTAYETLELG
     ADGVLLDTDE VDEIRKTVEV RDEMGRESLD LEYAEVTAIE QTGSADRVCI DTGSLMEHDE
     GMLVGSMARG LFFVHAETAE SPYVASRPFR VNAGAVHAYV RTPDGGTKYL SELQSGDEVQ
     IVDANGRTRE AIVGRAKIEK RPMFRVQAET EDSDRIETLL QNAETIKVHT QDGRTAVTDL
     EPGDEILIHH EDTATHFGER IEESIIEK